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BPT4:TERL

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Species (Taxon ID) Enterobacteria phage T4 (Bacteriophage T4). (10665)
Gene Name(s) 17
Protein Name(s) Terminase, large subunit

DNA-packaging protein Gp17 Gene product 17 gp17 Terminase large subunit

External Links
UniProt P17312
EMBL X52394
AF158101
AF158101
AF158101
AF158101
PIR JU0287
RefSeq NP_049776.1
NP_049777.1
NP_049778.1
NP_049779.1
PDB 2O0H
2O0J
2O0K
3CPE
3EZK
PDBsum 2O0H
2O0J
2O0K
3CPE
3EZK
ProteinModelPortal P17312
SMR P17312
DIP DIP-60322N
GeneID 1258545
1258647
1258656
1258675
EvolutionaryTrace P17312
Proteomes UP000009087
GO GO:0005524
GO:0004518
GO:0046797
GO:0019076
InterPro IPR027417
IPR004921
Pfam PF03237
SUPFAM SSF52540

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0046797

viral procapsid maturation

PMID:660719[1]

ECO:0000314

P

Figure 2

complete
CACAO 7040

GO:0016887

ATPase activity

PMID:19109896[2]

ECO:0000315

F

The ATPase protein was compared to two mutants (W533A and ΔS527G538) which had weakened interactions between their domains. The mutants were then compared to the wild-type with a Packaging ATPase assay. Both of the mutants had a loss of their ATPase activity. This is proven in figure 3e, where the concentration of cold ATP was increased every hour, for the wild-type and mutants. The third phosphate group was only cleaved in only the wild-type samples, which is seen in the appearance of the upper bands in the thin layer chromotherapy.

complete
CACAO 11500

Contributes to

GO:0043493

viral terminase complex

PMID:3294420[3]

ECO:0000314

C

gp16 and gp17 Terminase genes from T4 were over expressed in Ecoli bacteria in the presence of empty phage proheads in order to asses the headful DNA packaging abilities of the genes. Gp16 and gp17 were expressed individually and together in a complex. It was found that, "the gp16 function of the terminase complex is dispensable for packaging mature DNA, whereas gp17 is essential for packaging DNA under any condition tested." It was therefore determined that gp17 is the main Terminase protein in T4 necessary for the molecular function of DNA packaging.

complete
CACAO 11547

GO:0098009

virus terminase, large subunit

PMID:19109896[2]

ECO:0000314

C

Fig 1 of the paper illustrates gp17 as a large terminase.

complete
CACAO 11608

GO:0004518

nuclease activity

PMID:19109896[2]

ECO:0000314

F

The assay experiment of the gp17 terminase can be viewed in figure 3b. Lane's 0, 1, and 2 are how many hours after the addition of isopropyl β-D-1-thiogalactopyranoside (IPTG). This induces the expression of the DNA samples. The mutant sample are then compared to the known DNA. It is then compared to the mutant types, the mutant types did not have cleaved DNA. Proving its identity as a nuclease.

complete
CACAO 11955

GO:0043493

viral terminase complex

ECO:0000255

C

Terminate acts as a an ATP driven molecular motor for viral DNA translocation

Missing: with/from, reference
CACAO 12012

GO:0004536

deoxyribonuclease activity

PMID:19109896[2]

ECO:0000315

F

Figure 3b compares the mutant gp17 proteins to the wild types. Arg406 in T4 participates in binding DNA and nuclease activity. Mutant "Arg406Ala" showed that any substitutions in amino acids at the 406 position produced a null phenotype. Meaning that when they tested the phages in a plating assay the mutants failed to produce plaques. See figure 3b shows that unlike the wild-type, the mutant R406A did not degrade the DNA after 2 hours of incubation.

complete
CACAO 12014

involved_in

GO:0019072

viral genome packaging

PMID:18627466[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

PMID:18627466[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0098009

viral terminase, large subunit

PMID:18627466[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0046797

viral procapsid maturation

PMID:660719[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0032359

provirus excision

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1250

P

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Carrascosa, JL (1978) Head maturation pathway of bacteriophages T4 and T2. IV. In vitro transformation of T4 head-related particles produced by mutants in gene 17 to capsid-like structures. J. Virol. 26 420-8 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Sun, S et al. (2008) The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces. Cell 135 1251-62 PubMed GONUTS page
  3. Rao, VB & Black, LW (1988) Cloning, overexpression and purification of the terminase proteins gp16 and gp17 of bacteriophage T4. Construction of a defined in-vitro DNA packaging system using purified terminase proteins. J. Mol. Biol. 200 475-88 PubMed GONUTS page
  4. 4.0 4.1 4.2 Alam, TI et al. (2008) The headful packaging nuclease of bacteriophage T4. Mol. Microbiol. 69 1180-90 PubMed GONUTS page